ACHB_BOVIN
ID ACHB_BOVIN Reviewed; 505 AA.
AC P04758; A6QL86;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Acetylcholine receptor subunit beta;
DE Flags: Precursor;
GN Name=CHRNB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6548186; DOI=10.1111/j.1432-1033.1984.tb08424.x;
RA Tanabe T., Noda M., Furutani Y., Takai T., Takahashi H., Tanaka K.,
RA Hirose T., Inayama S., Numa S.;
RT "Primary structure of beta subunit precursor of calf muscle acetylcholine
RT receptor deduced from cDNA sequence.";
RL Eur. J. Biochem. 144:11-17(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane.
CC -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon
CC subunits interacts with the alpha-conotoxin ImII.
CC {ECO:0000250|UniProtKB:P11230}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-1/CHRNB1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X00962; CAA25475.1; -; mRNA.
DR EMBL; BC147876; AAI47877.1; -; mRNA.
DR PIR; S07227; S07227.
DR RefSeq; NP_776941.1; NM_174516.2.
DR RefSeq; XP_005220248.1; XM_005220191.3.
DR AlphaFoldDB; P04758; -.
DR SMR; P04758; -.
DR STRING; 9913.ENSBTAP00000025624; -.
DR PaxDb; P04758; -.
DR Ensembl; ENSBTAT00000025624; ENSBTAP00000025624; ENSBTAG00000019242.
DR GeneID; 282179; -.
DR KEGG; bta:282179; -.
DR CTD; 1140; -.
DR VEuPathDB; HostDB:ENSBTAG00000019242; -.
DR VGNC; VGNC:27330; CHRNB1.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158661; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P04758; -.
DR OMA; PCILITV; -.
DR OrthoDB; 776653at2759; -.
DR TreeFam; TF315605; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000019242; Expressed in biceps femoris and 104 other tissues.
DR ExpressionAtlas; P04758; baseline and differential.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0015267; F:channel activity; ISS:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0035095; P:behavioral response to nicotine; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; ISS:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISS:UniProtKB.
DR GO; GO:0001941; P:postsynaptic membrane organization; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISS:UniProtKB.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT CHAIN 25..505
FT /note="Acetylcholine receptor subunit beta"
FT /id="PRO_0000000314"
FT TOPO_DOM 25..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 365..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..166
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 57352 MW; B003D552A6701ECC CRC64;
MTPGALLLLL LGVLGAHLAP GARGSEAEGR LREKLFSGYD STVRPAREVG DRVWVSIGLT
LAQLISLNEK DEEMSTKVYL DLEWTDYRLS WDPEEHEGID SLRISAESVW LPDVVLLNNN
DGNFDVALDI NVVVSSDGSM RWQPPGIYRS SCSIQVTYFP FDWQNCTMVF SSYSYDSSEV
SLQTGLSPEG QERQEVYIHE GTFIENGQWE IIHKPSRLIQ PSVDPRGGGE GRREEVTFYL
IIRRKPLFYL VNVIAPCILI TLLAIFVFYL PPDAGEKMGL SIFALLTLTV FLLLLADKVP
ETSLSVPIII KYLMFTMVLV TFSVILSVVV LNLHHRSPHT HQMPLWVRQI FIHKLPLYLG
LKRPKPERDQ MQEPPSIAPR DSPGSGWGRG TDEYFIRKPP NDFLFPKPNR FQPELSAPDL
RRFIDGPNRA VGLPPELREV VSSISYIARQ LQEQEDHDVL KEDWQFVAMV VDRLFLWTFI
IFTSVGTLVI FLDATYHLPP ADPFP
